ID   IF3_THET8               Reviewed;         171 AA.
AC   Q5SKU2;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 2.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Translation initiation factor IF-3 {ECO:0000255|HAMAP-Rule:MF_00080};
GN   Name=infC {ECO:0000255|HAMAP-Rule:MF_00080};
GN   OrderedLocusNames=TTHA0551;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 83-171 WITH THE 30S RIBOSOMAL
RP   SUBUNIT.
RX   PubMed=11296217; DOI=10.1093/emboj/20.8.1829;
RA   Pioletti M., Schluenzen F., Harms J., Zarivach R., Gluehmann M., Avila H.,
RA   Bashan A., Bartels H., Auerbach T., Jacobi C., Hartsch T., Yonath A.,
RA   Franceschi F.;
RT   "Crystal structures of complexes of the small ribosomal subunit with
RT   tetracycline, edeine and IF3.";
RL   EMBO J. 20:1829-1839(2001).
CC   -!- FUNCTION: IF-3 binds to the 30S ribosomal subunit and shifts the
CC       equilibrium between 70S ribosomes and their 50S and 30S subunits in
CC       favor of the free subunits, thus enhancing the availability of 30S
CC       subunits on which protein synthesis initiation begins.
CC   -!- SUBUNIT: Monomer. Binds to proteins S7, S11 and S18 of the small
CC       ribosomal subunit.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the IF-3 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00080}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD70374.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AP008226; BAD70374.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_143817.1; NC_006461.1.
DR   PDB; 1I96; X-ray; 4.20 A; V=83-171.
DR   PDB; 5LMN; EM; 3.55 A; X=1-171.
DR   PDB; 5LMO; EM; 4.30 A; X=1-171.
DR   PDB; 5LMP; EM; 5.35 A; X=1-171.
DR   PDB; 5LMQ; EM; 4.20 A; X=1-171.
DR   PDB; 5LMR; EM; 4.45 A; X=1-171.
DR   PDB; 5LMS; EM; 5.10 A; X=1-171.
DR   PDB; 5LMT; EM; 4.15 A; X=1-171.
DR   PDB; 5LMU; EM; 4.00 A; X=1-171.
DR   PDB; 5LMV; EM; 4.90 A; X=1-171.
DR   PDBsum; 1I96; -.
DR   PDBsum; 5LMN; -.
DR   PDBsum; 5LMO; -.
DR   PDBsum; 5LMP; -.
DR   PDBsum; 5LMQ; -.
DR   PDBsum; 5LMR; -.
DR   PDBsum; 5LMS; -.
DR   PDBsum; 5LMT; -.
DR   PDBsum; 5LMU; -.
DR   PDBsum; 5LMV; -.
DR   AlphaFoldDB; Q5SKU2; -.
DR   EMDB; EMD-4073; -.
DR   EMDB; EMD-4074; -.
DR   EMDB; EMD-4075; -.
DR   EMDB; EMD-4076; -.
DR   EMDB; EMD-4077; -.
DR   EMDB; EMD-4078; -.
DR   EMDB; EMD-4079; -.
DR   EMDB; EMD-4080; -.
DR   EMDB; EMD-4083; -.
DR   SMR; Q5SKU2; -.
DR   EnsemblBacteria; BAD70374; BAD70374; BAD70374.
DR   KEGG; ttj:TTHA0551; -.
DR   PATRIC; fig|300852.9.peg.550; -.
DR   eggNOG; COG0290; Bacteria.
DR   HOGENOM; CLU_054919_3_2_0; -.
DR   EvolutionaryTrace; Q5SKU2; -.
DR   Proteomes; UP000000532; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.110.10; Translation initiation factor 3 (IF-3), C-terminal domain; 1.
DR   Gene3D; 3.10.20.80; Translation initiation factor 3 (IF-3), N-terminal domain; 1.
DR   HAMAP; MF_00080; IF_3; 1.
DR   InterPro; IPR036788; T_IF-3_C_sf.
DR   InterPro; IPR036787; T_IF-3_N_sf.
DR   InterPro; IPR001288; Translation_initiation_fac_3.
DR   InterPro; IPR019815; Translation_initiation_fac_3_C.
DR   InterPro; IPR019814; Translation_initiation_fac_3_N.
DR   NCBIfam; TIGR00168; infC; 1.
DR   PANTHER; PTHR10938; TRANSLATION INITIATION FACTOR IF-3; 1.
DR   PANTHER; PTHR10938:SF0; TRANSLATION INITIATION FACTOR IF-3, MITOCHONDRIAL; 1.
DR   Pfam; PF00707; IF3_C; 1.
DR   Pfam; PF05198; IF3_N; 1.
DR   SUPFAM; SSF55200; Translation initiation factor IF3, C-terminal domain; 1.
DR   SUPFAM; SSF54364; Translation initiation factor IF3, N-terminal domain; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Initiation factor; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..171
FT                   /note="Translation initiation factor IF-3"
FT                   /id="PRO_0000280033"
SQ   SEQUENCE   171 AA;  19866 MW;  55954FFC1E365E29 CRC64;
     MKEYLTNERI RAKQVRVVGP DGKQLGIMDT REALRLAQEM DLDLVLVGPN ADPPVARIMD
     YSKWRYEQQM AEKEARKKAK RTEVKSIKFR VKIDEHDYQT KLGHIKRFLQ EGHKVKVTIM
     FRGREVAHPE LGERILNRVT EDLKDLAVVE MKPEMLGRDM NMLLAPVKVS A
//